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Henrissat, B. (1991) A Classification of Glycosyl Hydrolases Based on Amino Acid Sequence Similarities. Biochemical Journal, 280, 309-316.

has been cited by the following article:

  • TITLE: Molecular Cloning of a Chitinase Gene from the Ovotestis of Kuroda’s Sea Hare Aplysia kurodai

    AUTHORS: Gaku Matsunaga, Syuuji Karasuda, Ryo Nishino, Hideto Fukushima, Masahiro Matsumiya

    KEYWORDS: Chitinase, Molecular Cloning, Kuroda’s Sea Hare Aplysia kurodai, Mollusc, Ovotestis, Phylogenetic Tree Analysis

    JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.7 No.1, January 29, 2016

    ABSTRACT: In this study, we report that we successfully cloned and sequenced a chitinase gene from the ovotestis of Kuroda’s sea hare Aplysia kurodai. By using reverse transcription-polymerase chain reaction (RT-PCR) and a system for the 5’ and 3’ rapid amplification of cDNA ends, we obtained a 1352 bp chitinase gene (AkChi) from the ovotestis of A. kurodai. AkChi contains a 1263 bp open reading frame that encodes 421 amino acids. The domain structure predicted from the deduced amino acid sequence was an N-terminal signal peptide and a catalytic domain of glycoside hydrolase (GH) family 18 chitinase. A comparative analysis of the deduced amino acid sequences of AkChi with those of the acidic mammalian chitinase of the California sea hare Aplysia californica revealed the highest homology at 83%. The purified chitinase from the ovotestis was digested by trypsin, and 119 residues of digested peptides were consistent with the deduced amino acid sequence of AkChi. We used RT-PCR to evaluate the expression of AkChi in various tissues of A. kurodai, and we observed that AkChi was expressed only in the ovotestis. A phylogenetic tree analysis, performed using the amino acid sequences of AkChi and known GH family 18 chitinases, showed that AkChi was separated from the molluscan chitinases with a chitin binding domain. To our knowledge, this is the first study demonstrating the cDNA cloning of an ovotestis chitinase from a sea hare.